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HEADER COMPLEX (SERINE PROTEASE/INHIBITOR) 03-NOV-95 1BCS 1BCS 2
TITLE COMPLEX OF THE WHEAT SERINE CARBOXYPEPTIDASE, CPDW-II, WITH 1BCS 3
TITLE 2 THE MICROBIAL PEPTIDE ALDEHYDE INHIBITOR, CHYMOSTATIN, AND 1BCS 4
TITLE 3 ARGININE AT 100 DEGREES KELVIN 1BCS 5
COMPND MOL_ID: 1; 1BCS 6
COMPND 2 MOLECULE: SERINE CARBOXYPEPTIDASE II; 1BCS 7
COMPND 3 CHAIN: A, B; 1BCS 8
COMPND 4 EC: 3.4.16.6; 1BCS 9
COMPND 5 MOL_ID: 2; 1BCS 10
COMPND 6 MOLECULE: ARGININE; 1BCS 11
COMPND 7 CHAIN: D; 1BCS 12
COMPND 8 ENGINEERED: YES; 1BCS 13
COMPND 9 HETEROGEN: CHYMOSTATIN A 1BCS 14
SOURCE MOL_ID: 1; 1BCS 15
SOURCE 2 ORGANISM_SCIENTIFIC: TRITICUM VULGARE; 1BCS 16
SOURCE 3 ORGANISM_COMMON: WHEAT; 1BCS 17
SOURCE 4 TISSUE: WHEAT GERM; 1BCS 18
SOURCE 5 MOL_ID: 2; 1BCS 19
SOURCE 6 SYNTHETIC: YES 1BCS 20
KEYWDS MICROBIAL PEPTIDE ALDEHYDE INHIBITOR 1BCS 21
EXPDTA X-RAY DIFFRACTION 1BCS 22
AUTHOR T.L.BULLOCK,S.J.REMINGTON 1BCS 23
REVDAT 1 08-MAR-96 1BCS 0 1BCS 24
JRNL AUTH T.L.BULLOCK,K.BREDDAM,S.J.REMINGTON 1BCS 25
JRNL TITL PEPTIDE ALDEHYDE COMPLEXES WITH WHEAT SERINE 1BCS 26
JRNL TITL 2 CARBOXYPEPTIDASE II 1BCS 27
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1BCS 28
JRNL REFN 0353 1BCS 29
REMARK 1 1BCS 30
REMARK 1 REFERENCE 1 1BCS 31
REMARK 1 AUTH T.L.BULLOCK,B.BRANCHAUD,S.J.REMINGTON 1BCS 32
REMARK 1 TITL STRUCTURE OF THE COMPLEX OF L-BENZYLSUCCINATE WITH 1BCS 33
REMARK 1 TITL 2 WHEAT SERINE CARBOXYPEPTIDASE AT 2.0 ANGSTROM 1BCS 34
REMARK 1 TITL 3 RESOLUTION 1BCS 35
REMARK 1 REF BIOCHEMISTRY V. 33 11127 1994 1BCS 36
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1BCS 37
REMARK 1 REFERENCE 2 1BCS 38
REMARK 1 AUTH D.I.LIAO,K.BREDDAM,R.M.SWEET,T.BULLOCK, 1BCS 39
REMARK 1 AUTH 2 S.J.REMINGTON 1BCS 40
REMARK 1 TITL REFINED ATOMIC MODEL OF WHEAT SERINE 1BCS 41
REMARK 1 TITL 2 CARBOXYPEPTIDASE II AT 2.2 ANGSTROM RESOLUTION 1BCS 42
REMARK 1 REF BIOCHEMISTRY V. 31 9796 1992 1BCS 43
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1BCS 44
REMARK 2 1BCS 45
REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1BCS 46
REMARK 3 1BCS 47
REMARK 3 REFINEMENT. 1BCS 48
REMARK 3 PROGRAM : TNT 1BCS 49
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS 1BCS 50
REMARK 3 1BCS 51
REMARK 3 MODEL QUALITY. 1BCS 52
REMARK 3 R VALUE (NO SIGMA CUTOFF) : 0.174 1BCS 53
REMARK 3 1BCS 54
REMARK 3 DATA USED IN REFINEMENT. 1BCS 55
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08 1BCS 56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33. 1BCS 57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 1BCS 58
REMARK 3 NUMBER OF REFLECTIONS : 46330 1BCS 59
REMARK 3 1BCS 60
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1BCS 61
REMARK 3 PROTEIN ATOMS : 3201 1BCS 62
REMARK 3 NUCLEIC ACID ATOMS : 0 1BCS 63
REMARK 3 HETEROGEN ATOMS : 530 1BCS 64
REMARK 3 SOLVENT ATOMS : 384 1BCS 65
REMARK 3 1BCS 66
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT 1BCS 67
REMARK 3 BOND LENGTHS (A) : 0.016 ; 0.020 ; 1BCS 68
REMARK 3 BOND ANGLES (DEGREES) : 2.85 ; 3. ; 1BCS 69
REMARK 3 GENERAL PLANES (A) : 0.019 ; 0.020 ; 1BCS 70
REMARK 3 1BCS 71
REMARK 3 1BCS 72
REMARK 3 DATA COLLECTION. 1BCS 73
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 46330 1BCS 74
REMARK 3 RESOLUTION RANGE 33.0 - 2.08 ANGSTROMS 1BCS 75
REMARK 3 COMPLETENESS OF DATA 86.5 % 1BCS 76
REMARK 3 REJECTION CRITERIA 0. SIGMA(I) 1BCS 77
REMARK 3 1BCS 78
REMARK 3 BOND DISTANCE 0.016(0.020) 1BCS 79
REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.019(0.020) 1BCS 80
REMARK 3 MULTIPLE TORSION CONTACT 0.042(0.1) 1BCS 81
REMARK 3 STAGGERED 16.9(15) 1BCS 82
REMARK 3 1BCS 83
REMARK 3 GEOMETRY LIBRARY PROVIDED WITH TNT 1BCS 84
REMARK 4 1BCS 85
REMARK 4 RESIDUES GLU A 24, ARG A 74, LYS A 163, ARG B 282, 1BCS 86
REMARK 4 VAL B 292, ASP B 375, GLN B 375A, AND GLN B 423 HAVE 1BCS 87
REMARK 4 INCOMPLETE SIDE CHAIN ATOMS. 1BCS 88
REMARK 5 1BCS 89
REMARK 5 SITE 1BCS 90
REMARK 5 SITE_IDENTIFIER: CAT 1BCS 91
REMARK 5 THREE RESIDUES FORMING THE CATALYTIC CENTER. 1BCS 92
REMARK 6 1BCS 93
REMARK 6 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED 1BCS 94
REMARK 6 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 1BCS 95
REMARK 6 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL 1BCS 96
REMARK 6 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE 1BCS 97
REMARK 6 NUMBER; I=INSERTION CODE): 1BCS 98
REMARK 6 1BCS 99
REMARK 6 M RES CSSEQI 1BCS 100
REMARK 6 0 HOH 351 DISTANCE = 6.83 ANGSTROMS 1BCS 101
REMARK 6 0 HOH 368 DISTANCE = 5.91 ANGSTROMS 1BCS 102
REMARK 6 0 HOH 391 DISTANCE = 5.94 ANGSTROMS 1BCS 103
REMARK 6 0 HOH 449 DISTANCE = 5.17 ANGSTROMS 1BCS 104
REMARK 18 1BCS 105
REMARK 18 EXPERIMENTAL DETAILS. 1BCS 106
REMARK 18 TEMPERATURE : 100 K 1BCS 107
REMARK 18 MONOCHROMATIC (Y/N) : Y 1BCS 108
REMARK 18 LAUE (Y/N) : N 1BCS 109
REMARK 18 WAVELENGTH OR RANGE (A) : 1.54 1BCS 110
REMARK 18 MONOCHROMATOR : GRAPHITE 1BCS 111
REMARK 18 DETECTOR TYPE : IMAGE PLATE/ R-AXIS 1BCS 112
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : R-AXIS 1BCS 113
REMARK 18 DATA REDUNDANCY : 2.75 1BCS 114
REMARK 18 MERGING R VALUE (INTENSITY) : 0.040 1BCS 115
REMARK 999 1BCS 116
REMARK 999 SEQUENCE 1BCS 117
REMARK 999 MODUSR: 1BCS SER A 146A THE OG ATOM IS LINKED VIA A 1BCS 118
REMARK 999 HEMIACETAL BOND TO THE CHYMOSTATIN MOLECULE 1BCS 119
REMARK 999 1BCS 120
REMARK 999 FOR CHAIN "A" - 5 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1BCS 121
REMARK 999 1BCS 122
REMARK 999 FOR CHAIN "A" - 3 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1BCS 123
REMARK 999 1BCS 124
REMARK 999 FOR CHAIN "B" - 2 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1BCS 125
REMARK 999 1BCS 126
REMARK 999 FOR CHAIN "B" - 5 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1BCS 127
DBREF 1BCS A -4 248 SWS P08819 CBP2_WHEAT 6 260 1BCS 128
DBREF 1BCS B 264 423 SWS P08819 CBP2_WHEAT 266 418 1BCS 129
SEQADV 1BCS B SWS P08819 GLN 370 GAP IN PDB ENTRY 1BCS 130
SEQRES 1 A 263 VAL GLU PRO SER GLY HIS ALA ALA ASP ARG ILE ALA ARG 1BCS 131
SEQRES 2 A 263 LEU PRO GLY GLN PRO ALA VAL ASP PHE ASP MET TYR SER 1BCS 132
SEQRES 3 A 263 GLY TYR ILE THR VAL ASP GLU GLY ALA GLY ARG SER LEU 1BCS 133
SEQRES 4 A 263 PHE TYR LEU LEU GLN GLU ALA PRO GLU ASP ALA GLN PRO 1BCS 134
SEQRES 5 A 263 ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY CYS 1BCS 135
SEQRES 6 A 263 SER SER VAL ALA TYR GLY ALA SER GLU GLU LEU GLY ALA 1BCS 136
SEQRES 7 A 263 PHE ARG VAL LYS PRO ARG GLY ALA GLY LEU VAL LEU ASN 1BCS 137
SEQRES 8 A 263 GLU TYR ARG TRP ASN LYS VAL ALA ASN VAL LEU PHE LEU 1BCS 138
SEQRES 9 A 263 ASP SER PRO ALA GLY VAL GLY PHE SER TYR THR ASN THR 1BCS 139
SEQRES 10 A 263 SER SER ASP ILE TYR THR SER GLY ASP ASN ARG THR ALA 1BCS 140
SEQRES 11 A 263 HIS ASP SER TYR ALA PHE LEU ALA LYS TRP PHE GLU ARG 1BCS 141
SEQRES 12 A 263 PHE PRO HIS TYR LYS TYR ARG ASP PHE TYR ILE ALA GLY 1BCS 142
SEQRES 13 A 263 GLU SER TYR ALA GLY HIS TYR VAL PRO GLU LEU SER GLN 1BCS 143
SEQRES 14 A 263 LEU VAL HIS ARG SER LYS ASN PRO VAL ILE ASN LEU LYS 1BCS 144
SEQRES 15 A 263 GLY PHE MET VAL GLY ASN GLY LEU ILE ASP ASP TYR HIS 1BCS 145
SEQRES 16 A 263 ASP TYR VAL GLY THR PHE GLU PHE TRP TRP ASN HIS GLY 1BCS 146
SEQRES 17 A 263 ILE VAL SER ASP ASP THR TYR ARG ARG LEU LYS GLU ALA 1BCS 147
SEQRES 18 A 263 CYS LEU HIS ASP SER PHE ILE HIS PRO SER PRO ALA CYS 1BCS 148
SEQRES 19 A 263 ASP ALA ALA THR ASP VAL ALA THR ALA GLU GLN GLY ASN 1BCS 149
SEQRES 20 A 263 ILE ASP MET TYR SER LEU TYR THR PRO VAL CYS ASN ILE 1BCS 150
SEQRES 21 A 263 THR SER SER 1BCS 151
SEQRES 1 B 160 THR GLY SER TYR ASP PRO CYS THR GLU ARG TYR SER THR 1BCS 152
SEQRES 2 B 160 ALA TYR TYR ASN ARG ARG ASP VAL GLN MET ALA LEU HIS 1BCS 153
SEQRES 3 B 160 ALA ASN VAL THR GLY ALA MET ASN TYR THR TRP ALA THR 1BCS 154
SEQRES 4 B 160 CYS SER ASP THR ILE ASN THR HIS TRP HIS ASP ALA PRO 1BCS 155
SEQRES 5 B 160 ARG SER MET LEU PRO ILE TYR ARG GLU LEU ILE ALA ALA 1BCS 156
SEQRES 6 B 160 GLY LEU ARG ILE TRP VAL PHE SER GLY ASP THR ASP ALA 1BCS 157
SEQRES 7 B 160 VAL VAL PRO LEU THR ALA THR ARG TYR SER ILE GLY ALA 1BCS 158
SEQRES 8 B 160 LEU GLY LEU PRO THR THR THR SER TRP TYR PRO TRP TYR 1BCS 159
SEQRES 9 B 160 ASP ASP GLN GLU VAL GLY GLY TRP SER GLN VAL TYR LYS 1BCS 160
SEQRES 10 B 160 GLY LEU THR LEU VAL SER VAL ARG GLY ALA GLY HIS GLU 1BCS 161
SEQRES 11 B 160 VAL PRO LEU HIS ARG PRO ARG GLN ALA LEU VAL LEU PHE 1BCS 162
SEQRES 12 B 160 GLN TYR PHE LEU GLN GLY LYS PRO MET PRO GLY GLN THR 1BCS 163
SEQRES 13 B 160 LYS ASN ALA THR 1BCS 164
SEQRES 1 D 1 ARG 1BCS 165
FTNOTE 1 1BCS 166
FTNOTE 1 CIS PROLINE - PRO A 43 1BCS 167
FTNOTE 2 1BCS 168
FTNOTE 2 CIS PROLINE - PRO A 54 1BCS 169
FTNOTE 3 1BCS 170
FTNOTE 3 CIS PROLINE - PRO A 96 1BCS 171
HET GOL 450 6 GLYCEROL 1BCS 172
HET ACT 461 4 ACETATE ION 1BCS 173
HET CST 500 44 CHYMOSTATIN A 1BCS 174
HET NAG 1131 14 N-ACETYL-D-GLUCOSAMINE 1BCS 175
HET FUC 105 10 FUCOSE 1BCS 176
HET NAG 1051 14 N-ACETYL-D-GLUCOSAMINE 1BCS 177
HET NAG 1052 14 N-ACETYL-D-GLUCOSAMINE 1BCS 178
HET NAG 2911 14 N-ACETYL-D-GLUCOSAMINE 1BCS 179
HET NAG 2912 14 N-ACETYL-D-GLUCOSAMINE 1BCS 180
FORMUL 4 GOL C3 H8 O3 1BCS 181
FORMUL 5 ACT C2 H3 O2 1- 1BCS 182
FORMUL 6 CST C31 H41 N7 O6 1BCS 183
FORMUL 7 NAG 5(C8 H15 N1 O6) 1BCS 184
FORMUL 8 FUC C6 H12 O6 1BCS 185
FORMUL 9 HOH *384(H2 O1) 1BCS 186
HELIX 1 1 ALA A -3 ASP A -1 5 1BCS 187
HELIX 2 2 GLU A 39 ALA A 41 5 1BCS 188
HELIX 3 3 GLY A 61 GLU A 64 1 1BCS 189
HELIX 4 4 PRO A 73 GLY A 75 5 1BCS 190
HELIX 5 5 TRP A 84 LYS A 86 5 1BCS 191
HELIX 6 6 SER A 107 TYR A 111 5 1BCS 192
HELIX 7 7 ASP A 112C ARG A 129 1 1BCS 193
HELIX 8 8 PRO A 131 TYR A 133 5 1BCS 194
HELIX 9 9 SER A 146 SER A 162 5 1BCS 195
HELIX 10 10 ASP A 181 HIS A 195 1 1BCS 196
HELIX 11 11 ASP A 200 CYS A 210 1 1BCS 197
HELIX 12 12 PRO A 220 GLN A 233 1 1BCS 198
HELIX 13 13 THR B 271 TYR B 279 1 1BCS 199
HELIX 14 14 ARG B 282 LEU B 288 1 1BCS 200
HELIX 15 15 ASP B 303B HIS B 308 1 1BCS 201
HELIX 16 16 LEU B 314 ALA B 322 1 1BCS 202
HELIX 17 17 LEU B 343 LEU B 353 1 1BCS 203
HELIX 18 18 VAL B 399 HIS B 402 1 1BCS 204
HELIX 19 19 PRO B 404 GLN B 416 1 1BCS 205
SHEET 1 A10 TYR B 370 ASP B 374 0 1BCS 206
SHEET 2 A10 GLU B 376 TYR B 384 -1 N SER B 381 O TYR B 370 1BCS 207
SHEET 3 A10 LEU B 387 VAL B 392 -1 N LEU B 389 O GLN B 382 1BCS 208
SHEET 4 A10 ARG B 329 GLY B 335 1 N VAL B 332 O THR B 388 1BCS 209
SHEET 5 A10 ASN A 168 GLY A 175 1 N PHE A 172 O ARG B 329 1BCS 210
SHEET 6 A10 ASP A 139 GLU A 145 1 N PHE A 140 O ASN A 168 1BCS 211
SHEET 7 A10 LEU A 46 LEU A 50 1 N LEU A 46 O TYR A 141 1BCS 212
SHEET 8 A10 ASN A 89 LEU A 93 1 N ASN A 89 O VAL A 47 1BCS 213
SHEET 9 A10 ARG A 28 GLN A 35 -1 N GLN A 35 O VAL A 90 1BCS 214
SHEET 10 A10 MET A 16 ASP A 23A-1 N ASP A 23A O ARG A 28 1BCS 215
SHEET 1 B 2 PHE A 69 VAL A 71 0 1BCS 216
SHEET 2 B 2 LEU A 77 LEU A 79 -1 N VAL A 78 O ARG A 70 1BCS 217
SSBOND 1 CYS A 56 CYS B 303 1BCS 218
SSBOND 2 CYS A 210 CYS A 222 1BCS 219
SSBOND 3 CYS A 246 CYS B 268 1BCS 220
SITE 1 CAT 3 ASP B 338 HIS B 397 SER A 146 1BCS 221
CRYST1 95.400 95.400 208.300 90.00 90.00 90.00 P 41 21 2 16 1BCS 222
ORIGX1 1.000000 0.000000 0.000000 0.00000 1BCS 223
ORIGX2 0.000000 1.000000 0.000000 0.00000 1BCS 224
ORIGX3 0.000000 0.000000 1.000000 0.00000 1BCS 225
SCALE1 0.010482 0.000000 0.000000 0.00000 1BCS 226
SCALE2 0.000000 0.010482 0.000000 0.00000 1BCS 227
SCALE3 0.000000 0.000000 0.004801 0.00000 1BCS 228 |